GenomeNet

Database: UniProt/SWISS-PROT
Entry: RPOM_HUMAN
LinkDB: RPOM_HUMAN
Original site: RPOM_HUMAN 
ID   RPOM_HUMAN              Reviewed;        1230 AA.
AC   O00411; O60370;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 2.
DT   20-JUN-2018, entry version 166.
DE   RecName: Full=DNA-directed RNA polymerase, mitochondrial;
DE            Short=MtRPOL;
DE            EC=2.7.7.6;
DE   Flags: Precursor;
GN   Name=POLRMT;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   PubMed=9097968; DOI=10.1093/hmg/6.4.615;
RA   Tiranti V., Savoia A., Forti F., D'Apolito M.F., Centra M., Rocchi M.,
RA   Zeviani M.;
RT   "Identification of the gene encoding the human mitochondrial RNA
RT   polymerase (h-mtRPOL) by cyberscreening of the Expressed Sequence Tags
RT   database.";
RL   Hum. Mol. Genet. 6:615-625(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15057824; DOI=10.1038/nature02399;
RA   Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
RA   Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
RA   Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
RA   Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
RA   Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
RA   Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
RA   Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
RA   Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
RA   Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
RA   Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
RA   Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
RA   Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
RA   Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
RA   Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
RA   Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
RA   Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA   Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA   Rubin E.M., Lucas S.M.;
RT   "The DNA sequence and biology of human chromosome 19.";
RL   Nature 428:529-535(2004).
RN   [3]
RP   INTERACTION WITH TFB1M AND TFB2M.
RX   PubMed=12068295; DOI=10.1038/ng909;
RA   Falkenberg M., Gaspari M., Rantanen A., Trifunovic A., Larsson N.-G.,
RA   Gustafsson C.M.;
RT   "Mitochondrial transcription factors B1 and B2 activate transcription
RT   of human mtDNA.";
RL   Nat. Genet. 31:289-294(2002).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA   Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [5]
RP   FUNCTION, AND INTERACTION WITH TEFM.
RX   PubMed=21278163; DOI=10.1093/nar/gkq1224;
RA   Minczuk M., He J., Duch A.M., Ettema T.J., Chlebowski A., Dzionek K.,
RA   Nijtmans L.G., Huynen M.A., Holt I.J.;
RT   "TEFM (c17orf42) is necessary for transcription of human mtDNA.";
RL   Nucleic Acids Res. 39:4284-4299(2011).
RN   [6]
RP   IDENTIFICATION IN A COMPLEX WITH SIRT3 AND FOXO3, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=23283301; DOI=10.1007/s00018-012-1244-6;
RA   Peserico A., Chiacchiera F., Grossi V., Matrone A., Latorre D.,
RA   Simonatto M., Fusella A., Ryall J.G., Finley L.W., Haigis M.C.,
RA   Villani G., Puri P.L., Sartorelli V., Simone C.;
RT   "A novel AMPK-dependent FoxO3A-SIRT3 intramitochondrial complex
RT   sensing glucose levels.";
RL   Cell. Mol. Life Sci. 70:2015-2029(2013).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
RA   Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
RN   [8]
RP   IDENTIFICATION IN A COMPLEX WITH SIRT3; TFAM AND FOXO3, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=29445193; DOI=10.1038/s41419-018-0336-0;
RA   Celestini V., Tezil T., Russo L., Fasano C., Sanese P., Forte G.,
RA   Peserico A., Lepore Signorile M., Longo G., De Rasmo D., Signorile A.,
RA   Gadaleta R.M., Scialpi N., Terao M., Garattini E., Cocco T.,
RA   Villani G., Moschetta A., Grossi V., Simone C.;
RT   "Uncoupling FoxO3A mitochondrial and nuclear functions in cancer cells
RT   undergoing metabolic stress and chemotherapy.";
RL   Cell Death Dis. 9:231-231(2018).
CC   -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription
CC       of mitochondrial DNA into RNA using the four ribonucleoside
CC       triphosphates as substrates. {ECO:0000269|PubMed:21278163}.
CC   -!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate
CC       + RNA(n+1). {ECO:0000255|PROSITE-ProRule:PRU10031,
CC       ECO:0000255|PROSITE-ProRule:PRU10032}.
CC   -!- SUBUNIT: Upon metabolic stress, forms a complex composed of FOXO3,
CC       SIRT3 and mitochondrial RNA polymerase POLRMT; the complex is
CC       recruited to mtDNA in a SIRT3-dependent manner (PubMed:23283301).
CC       Also forms a complex composed of FOXO3, SIRT3, TFAM and POLRMT
CC       (PubMed:29445193). Interacts with TFB1M and TFB2M, leading to the
CC       stimulation of transcription (PubMed:12068295). Interacts with
CC       TEFM (PubMed:21278163). {ECO:0000269|PubMed:12068295,
CC       ECO:0000269|PubMed:21278163, ECO:0000269|PubMed:23283301,
CC       ECO:0000269|PubMed:29445193}.
CC   -!- INTERACTION:
CC       P52815:MRPL12; NbExp=4; IntAct=EBI-355145, EBI-358272;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:23283301,
CC       ECO:0000269|PubMed:29445193}.
CC   -!- SIMILARITY: Belongs to the phage and mitochondrial RNA polymerase
CC       family. {ECO:0000305}.
DR   EMBL; U75370; AAB58255.1; -; mRNA.
DR   EMBL; AC004449; AAC06147.1; -; Genomic_DNA.
DR   CCDS; CCDS12036.1; -.
DR   RefSeq; NP_005026.3; NM_005035.3.
DR   UniGene; Hs.254113; -.
DR   PDB; 3SPA; X-ray; 2.50 A; A=105-1230.
DR   PDB; 4BOC; X-ray; 2.65 A; A=151-1230.
DR   PDB; 5OLA; X-ray; 3.90 A; E/F=151-1230.
DR   PDB; 6ERP; X-ray; 4.50 A; A/B=105-1230.
DR   PDB; 6ERQ; X-ray; 4.50 A; A/B=105-1230.
DR   PDBsum; 3SPA; -.
DR   PDBsum; 4BOC; -.
DR   PDBsum; 5OLA; -.
DR   PDBsum; 6ERP; -.
DR   PDBsum; 6ERQ; -.
DR   ProteinModelPortal; O00411; -.
DR   SMR; O00411; -.
DR   BioGrid; 111438; 41.
DR   DIP; DIP-56412N; -.
DR   IntAct; O00411; 19.
DR   MINT; O00411; -.
DR   STRING; 9606.ENSP00000215591; -.
DR   ChEMBL; CHEMBL3120041; -.
DR   iPTMnet; O00411; -.
DR   PhosphoSitePlus; O00411; -.
DR   BioMuta; POLRMT; -.
DR   EPD; O00411; -.
DR   MaxQB; O00411; -.
DR   PaxDb; O00411; -.
DR   PeptideAtlas; O00411; -.
DR   PRIDE; O00411; -.
DR   ProteomicsDB; 47875; -.
DR   Ensembl; ENST00000588649; ENSP00000465759; ENSG00000099821.
DR   GeneID; 5442; -.
DR   KEGG; hsa:5442; -.
DR   UCSC; uc002lpf.2; human.
DR   CTD; 5442; -.
DR   DisGeNET; 5442; -.
DR   EuPathDB; HostDB:ENSG00000099821.13; -.
DR   GeneCards; POLRMT; -.
DR   H-InvDB; HIX0027511; -.
DR   H-InvDB; HIX0059707; -.
DR   HGNC; HGNC:9200; POLRMT.
DR   HPA; HPA006366; -.
DR   MIM; 601778; gene.
DR   neXtProt; NX_O00411; -.
DR   OpenTargets; ENSG00000099821; -.
DR   PharmGKB; PA33522; -.
DR   eggNOG; KOG1038; Eukaryota.
DR   eggNOG; COG5108; LUCA.
DR   GeneTree; ENSGT00390000008060; -.
DR   HOGENOM; HOG000044061; -.
DR   HOVERGEN; HBG078730; -.
DR   InParanoid; O00411; -.
DR   KO; K10908; -.
DR   OMA; DWFTECA; -.
DR   OrthoDB; EOG091G00YJ; -.
DR   PhylomeDB; O00411; -.
DR   TreeFam; TF105700; -.
DR   Reactome; R-HSA-163282; Mitochondrial transcription initiation.
DR   Reactome; R-HSA-2151201; Transcriptional activation of mitochondrial biogenesis.
DR   GeneWiki; POLRMT; -.
DR   GenomeRNAi; 5442; -.
DR   PRO; PR:O00411; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   Bgee; ENSG00000099821; -.
DR   CleanEx; HS_POLRMT; -.
DR   ExpressionAtlas; O00411; baseline and differential.
DR   Genevisible; O00411; HS.
DR   GO; GO:0034245; C:mitochondrial DNA-directed RNA polymerase complex; IBA:GO_Central.
DR   GO; GO:0005759; C:mitochondrial matrix; IDA:UniProtKB.
DR   GO; GO:0042645; C:mitochondrial nucleoid; IDA:BHF-UCL.
DR   GO; GO:0005739; C:mitochondrion; IDA:HGNC.
DR   GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR   GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IDA:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR   GO; GO:0006390; P:mitochondrial transcription; IDA:UniProtKB.
DR   GO; GO:0007005; P:mitochondrion organization; TAS:Reactome.
DR   GO; GO:0006391; P:transcription initiation from mitochondrial promoter; TAS:Reactome.
DR   Gene3D; 1.10.1320.10; -; 1.
DR   Gene3D; 1.25.40.10; -; 1.
DR   InterPro; IPR002092; DNA-dir_Rpol_phage-type.
DR   InterPro; IPR037159; RNA_POL_N_sf.
DR   InterPro; IPR029262; RPOL_N.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   PANTHER; PTHR10102; PTHR10102; 1.
DR   Pfam; PF00940; RNA_pol; 1.
DR   Pfam; PF14700; RPOL_N; 1.
DR   SMART; SM01311; RPOL_N; 1.
DR   PROSITE; PS00900; RNA_POL_PHAGE_1; 1.
DR   PROSITE; PS00489; RNA_POL_PHAGE_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Complete proteome; DNA-directed RNA polymerase;
KW   Mitochondrion; Nucleotidyltransferase; Polymorphism;
KW   Reference proteome; Transcription; Transferase; Transit peptide.
FT   TRANSIT       1     41       Mitochondrion. {ECO:0000255}.
FT   CHAIN        42   1230       DNA-directed RNA polymerase,
FT                                mitochondrial.
FT                                /FTId=PRO_0000031068.
FT   REGION      802   1230       Mediates interaction with TEFM.
FT                                {ECO:0000269|PubMed:21278163}.
FT   ACT_SITE    922    922       {ECO:0000250}.
FT   ACT_SITE    991    991       {ECO:0000250}.
FT   ACT_SITE   1151   1151       {ECO:0000250}.
FT   VARIANT     555    555       E -> A (in dbSNP:rs2238549).
FT                                /FTId=VAR_019427.
FT   CONFLICT    399    399       L -> F (in Ref. 1; AAB58255).
FT                                {ECO:0000305}.
FT   CONFLICT    983    983       G -> S (in Ref. 1; AAB58255).
FT                                {ECO:0000305}.
FT   HELIX       221    236       {ECO:0000244|PDB:3SPA}.
FT   HELIX       239    251       {ECO:0000244|PDB:3SPA}.
FT   HELIX       253    256       {ECO:0000244|PDB:3SPA}.
FT   HELIX       261    274       {ECO:0000244|PDB:3SPA}.
FT   HELIX       277    289       {ECO:0000244|PDB:3SPA}.
FT   HELIX       296    309       {ECO:0000244|PDB:3SPA}.
FT   HELIX       313    325       {ECO:0000244|PDB:3SPA}.
FT   HELIX       331    336       {ECO:0000244|PDB:3SPA}.
FT   HELIX       341    351       {ECO:0000244|PDB:3SPA}.
FT   HELIX       352    354       {ECO:0000244|PDB:3SPA}.
FT   TURN        372    374       {ECO:0000244|PDB:3SPA}.
FT   HELIX       375    378       {ECO:0000244|PDB:3SPA}.
FT   STRAND      380    382       {ECO:0000244|PDB:4BOC}.
FT   HELIX       393    409       {ECO:0000244|PDB:3SPA}.
FT   STRAND      411    415       {ECO:0000244|PDB:3SPA}.
FT   HELIX       427    461       {ECO:0000244|PDB:3SPA}.
FT   HELIX       469    472       {ECO:0000244|PDB:3SPA}.
FT   HELIX       476    489       {ECO:0000244|PDB:3SPA}.
FT   HELIX       497    519       {ECO:0000244|PDB:3SPA}.
FT   HELIX       522    533       {ECO:0000244|PDB:3SPA}.
FT   HELIX       534    536       {ECO:0000244|PDB:3SPA}.
FT   HELIX       549    557       {ECO:0000244|PDB:3SPA}.
FT   HELIX       562    564       {ECO:0000244|PDB:3SPA}.
FT   HELIX       569    586       {ECO:0000244|PDB:3SPA}.
FT   STRAND      588    590       {ECO:0000244|PDB:4BOC}.
FT   STRAND      604    610       {ECO:0000244|PDB:3SPA}.
FT   STRAND      613    616       {ECO:0000244|PDB:4BOC}.
FT   STRAND      619    623       {ECO:0000244|PDB:3SPA}.
FT   HELIX       625    634       {ECO:0000244|PDB:3SPA}.
FT   STRAND      637    642       {ECO:0000244|PDB:3SPA}.
FT   HELIX       643    645       {ECO:0000244|PDB:3SPA}.
FT   STRAND      648    650       {ECO:0000244|PDB:3SPA}.
FT   STRAND      653    657       {ECO:0000244|PDB:3SPA}.
FT   STRAND      660    666       {ECO:0000244|PDB:3SPA}.
FT   HELIX       677    685       {ECO:0000244|PDB:3SPA}.
FT   HELIX       689    692       {ECO:0000244|PDB:3SPA}.
FT   HELIX       693    703       {ECO:0000244|PDB:3SPA}.
FT   STRAND      706    709       {ECO:0000244|PDB:3SPA}.
FT   HELIX       711    721       {ECO:0000244|PDB:3SPA}.
FT   TURN        722    724       {ECO:0000244|PDB:3SPA}.
FT   HELIX       727    729       {ECO:0000244|PDB:3SPA}.
FT   HELIX       735    737       {ECO:0000244|PDB:4BOC}.
FT   STRAND      748    750       {ECO:0000244|PDB:4BOC}.
FT   HELIX       772    789       {ECO:0000244|PDB:3SPA}.
FT   STRAND      798    800       {ECO:0000244|PDB:3SPA}.
FT   STRAND      806    809       {ECO:0000244|PDB:3SPA}.
FT   STRAND      811    813       {ECO:0000244|PDB:3SPA}.
FT   HELIX       819    823       {ECO:0000244|PDB:3SPA}.
FT   STRAND      825    829       {ECO:0000244|PDB:3SPA}.
FT   TURN        834    836       {ECO:0000244|PDB:3SPA}.
FT   HELIX       837    849       {ECO:0000244|PDB:3SPA}.
FT   HELIX       857    876       {ECO:0000244|PDB:3SPA}.
FT   TURN        878    880       {ECO:0000244|PDB:3SPA}.
FT   HELIX       884    887       {ECO:0000244|PDB:3SPA}.
FT   STRAND      888    890       {ECO:0000244|PDB:3SPA}.
FT   HELIX       891    905       {ECO:0000244|PDB:3SPA}.
FT   STRAND      907    909       {ECO:0000244|PDB:3SPA}.
FT   HELIX       910    912       {ECO:0000244|PDB:3SPA}.
FT   STRAND      918    922       {ECO:0000244|PDB:3SPA}.
FT   HELIX       926    934       {ECO:0000244|PDB:3SPA}.
FT   HELIX       938    943       {ECO:0000244|PDB:3SPA}.
FT   HELIX       955    972       {ECO:0000244|PDB:3SPA}.
FT   HELIX       976    980       {ECO:0000244|PDB:3SPA}.
FT   TURN        981    983       {ECO:0000244|PDB:3SPA}.
FT   HELIX       987    999       {ECO:0000244|PDB:3SPA}.
FT   STRAND     1002   1004       {ECO:0000244|PDB:3SPA}.
FT   HELIX      1005   1015       {ECO:0000244|PDB:3SPA}.
FT   STRAND     1018   1020       {ECO:0000244|PDB:4BOC}.
FT   TURN       1022   1024       {ECO:0000244|PDB:3SPA}.
FT   HELIX      1025   1043       {ECO:0000244|PDB:3SPA}.
FT   HELIX      1045   1063       {ECO:0000244|PDB:3SPA}.
FT   STRAND     1069   1071       {ECO:0000244|PDB:3SPA}.
FT   STRAND     1077   1079       {ECO:0000244|PDB:3SPA}.
FT   HELIX      1112   1141       {ECO:0000244|PDB:3SPA}.
FT   STRAND     1147   1149       {ECO:0000244|PDB:3SPA}.
FT   STRAND     1152   1156       {ECO:0000244|PDB:3SPA}.
FT   HELIX      1157   1159       {ECO:0000244|PDB:3SPA}.
FT   HELIX      1160   1176       {ECO:0000244|PDB:3SPA}.
FT   HELIX      1179   1191       {ECO:0000244|PDB:3SPA}.
FT   HELIX      1198   1209       {ECO:0000244|PDB:3SPA}.
FT   HELIX      1219   1224       {ECO:0000244|PDB:3SPA}.
FT   STRAND     1228   1230       {ECO:0000244|PDB:4BOC}.
SQ   SEQUENCE   1230 AA;  138620 MW;  47AFBF2E0884AEFA CRC64;
     MSALCWGRGA AGLKRALRPC GRPGLPGKEG TAGGVCGPRR SSSASPQEQD QDRRKDWGHV
     ELLEVLQARV RQLQAESVSE VVVNRVDVAR LPECGSGDGS LQPPRKVQMG AKDATPVPCG
     RWAKILEKDK RTQQMRMQRL KAKLQMPFQS GEFKALTRRL QVEPRLLSKQ MAGCLEDCTR
     QAPESPWEEQ LARLLQEAPG KLSLDVEQAP SGQHSQAQLS GQQQRLLAFF KCCLLTDQLP
     LAHHLLVVHH GQRQKRKLLT LDMYNAVMLG WARQGAFKEL VYVLFMVKDA GLTPDLLSYA
     AALQCMGRQD QDAGTIERCL EQMSQEGLKL QALFTAVLLS EEDRATVLKA VHKVKPTFSL
     PPQLPPPVNT SKLLRDVYAK DGRVSYPKLH LPLKTLQCLF EKQLHMELAS RVCVVSVEKP
     TLPSKEVKHA RKTLKTLRDQ WEKALCRALR ETKNRLEREV YEGRFSLYPF LCLLDEREVV
     RMLLQVLQAL PAQGESFTTL ARELSARTFS RHVVQRQRVS GQVQALQNHY RKYLCLLASD
     AEVPEPCLPR QYWEELGAPE ALREQPWPLP VQMELGKLLA EMLVQATQMP CSLDKPHRSS
     RLVPVLYHVY SFRNVQQIGI LKPHPAYVQL LEKAAEPTLT FEAVDVPMLC PPLPWTSPHS
     GAFLLSPTKL MRTVEGATQH QELLETCPPT ALHGALDALT QLGNCAWRVN GRVLDLVLQL
     FQAKGCPQLG VPAPPSEAPQ PPEAHLPHSA APARKAELRR ELAHCQKVAR EMHSLRAEAL
     YRLSLAQHLR DRVFWLPHNM DFRGRTYPCP PHFNHLGSDV ARALLEFAQG RPLGPHGLDW
     LKIHLVNLTG LKKREPLRKR LAFAEEVMDD ILDSADQPLT GRKWWMGAEE PWQTLACCME
     VANAVRASDP AAYVSHLPVH QDGSCNGLQH YAALGRDSVG AASVNLEPSD VPQDVYSGVA
     AQVEVFRRQD AQRGMRVAQV LEGFITRKVV KQTVMTVVYG VTRYGGRLQI EKRLRELSDF
     PQEFVWEASH YLVRQVFKSL QEMFSGTRAI QHWLTESARL ISHMGSVVEW VTPLGVPVIQ
     PYRLDSKVKQ IGGGIQSITY THNGDISRKP NTRKQKNGFP PNFIHSLDSS HMMLTALHCY
     RKGLTFVSVH DCYWTHAADV SVMNQVCREQ FVRLHSEPIL QDLSRFLVKR FCSEPQKILE
     ASQLKETLQA VPKPGAFDLE QVKRSTYFFS
//
DBGET integrated database retrieval system